The heat stability of rapeseed 12s globulin (cruciferin) was examined using 8-anilinonaphthalene-l-sulphonic acid (ANS) as a fluorescence probe. Heating cruciferin (0.06-0.3 mg ml-in 10 mM glycyl-glycyl piperizine buffer, pH 7.0, with 0.1-1.0 M NaCl) for 20 min increased its hydrophobicity as monito
Solubility of the 12 S globulin from rapeseed effected by phytic acid
✍ Scribed by Schwenke, K. D. ;Elkowicz, K. ;Kozłowska, H.
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 149 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0027-769X
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✦ Synopsis
The solubility profile is one of the characteristics of plant protein isolates. It depends on the nature of the protein (e.g. the isoelectric point), on the technolcgical procedure (extraction, precipitation, drying etc), and also on the interaction of the protein with other substances (1). Phytic acid is one of the most
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## Academy of Sciences of the German Democratic Republic A reversible dissociation of the 12 S globulin from rapeseed (Brassica napus L.) depending on ionic strength (Short communication)
The 12 S globulin is an oligomeric storage protein in rapeseed with a molecular weight of 300 000 g . m1-l (1, 2 ) . Its molecular shape and quaternary structure has been investigated by means of small-angle X-ray scattering and by electron microscopy after negative staining (2 -4). The object